RGS6_MOUSE
ID RGS6_MOUSE Reviewed; 472 AA.
AC Q9Z2H2; Q08AT5; Q8BGI8;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Regulator of G-protein signaling 6;
DE Short=RGS6;
GN Name=Rgs6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 64-472.
RA He W., Wensel T.G.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH RGS7BP.
RX PubMed=15632198; DOI=10.1074/jbc.c400596200;
RA Martemyanov K.A., Yoo P.J., Skiba N.P., Arshavsky V.Y.;
RT "R7BP, a novel neuronal protein interacting with RGS proteins of the R7
RT family.";
RL J. Biol. Chem. 280:5133-5136(2005).
RN [5]
RP INTERACTION WITH RGS7BP, AND SUBCELLULAR LOCATION.
RX PubMed=15897264; DOI=10.1083/jcb.200502007;
RA Drenan R.M., Doupnik C.A., Boyle M.P., Muglia L.J., Huettner J.E.,
RA Linder M.E., Blumer K.J.;
RT "Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a
RT novel membrane anchor for the RGS7 family.";
RL J. Cell Biol. 169:623-633(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades.
CC Inhibits signal transduction by increasing the GTPase activity of G
CC protein alpha subunits, thereby driving them into their inactive GDP-
CC bound form. The RGS6/GNB5 dimer enhances GNAO1 GTPase activity.
CC {ECO:0000250|UniProtKB:P49758}.
CC -!- SUBUNIT: Interacts with GNB5 (By similarity). Interacts with RGS7BP,
CC leading to regulate the subcellular location of the heterodimer formed
CC with GNB5 (PubMed:15632198, PubMed:15897264). Interacts with GNAI1 (By
CC similarity). {ECO:0000250|UniProtKB:P49758,
CC ECO:0000269|PubMed:15632198, ECO:0000269|PubMed:15897264}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15897264}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49758}. Membrane
CC {ECO:0000250|UniProtKB:P49758}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49758}. Nucleus {ECO:0000250|UniProtKB:P49758}.
CC Cell membrane {ECO:0000269|PubMed:15897264}. Note=Interaction with GNB5
CC mediates translocation to the nucleus. {ECO:0000250|UniProtKB:P49758}.
CC -!- DOMAIN: The RGS domain interacts avidly with Galpha and mediates the
CC acceleration of Galpha-mediated GTP hydrolysis. {ECO:0000250}.
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DR EMBL; AK052527; BAC35026.1; -; mRNA.
DR EMBL; AK053087; BAC35262.1; -; mRNA.
DR EMBL; BC125029; AAI25030.1; -; mRNA.
DR EMBL; BC125030; AAI25031.1; -; mRNA.
DR EMBL; AF061933; AAC70011.1; -; mRNA.
DR CCDS; CCDS79132.1; -.
DR RefSeq; NP_001268990.1; NM_001282061.2.
DR RefSeq; NP_001297407.1; NM_001310478.2.
DR RefSeq; NP_056627.1; NM_015812.4.
DR AlphaFoldDB; Q9Z2H2; -.
DR SMR; Q9Z2H2; -.
DR BioGRID; 206111; 2.
DR IntAct; Q9Z2H2; 1.
DR STRING; 10090.ENSMUSP00000140701; -.
DR iPTMnet; Q9Z2H2; -.
DR PhosphoSitePlus; Q9Z2H2; -.
DR MaxQB; Q9Z2H2; -.
DR PaxDb; Q9Z2H2; -.
DR PRIDE; Q9Z2H2; -.
DR ProteomicsDB; 255254; -.
DR Antibodypedia; 145; 135 antibodies from 25 providers.
DR DNASU; 50779; -.
DR Ensembl; ENSMUST00000186458; ENSMUSP00000139735; ENSMUSG00000021219.
DR Ensembl; ENSMUST00000200911; ENSMUSP00000143801; ENSMUSG00000021219.
DR Ensembl; ENSMUST00000202210; ENSMUSP00000143961; ENSMUSG00000021219.
DR GeneID; 50779; -.
DR KEGG; mmu:50779; -.
DR UCSC; uc007oda.2; mouse.
DR CTD; 9628; -.
DR MGI; MGI:1354730; Rgs6.
DR VEuPathDB; HostDB:ENSMUSG00000021219; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000157159; -.
DR InParanoid; Q9Z2H2; -.
DR OrthoDB; 415625at2759; -.
DR PhylomeDB; Q9Z2H2; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR BioGRID-ORCS; 50779; 0 hits in 51 CRISPR screens.
DR ChiTaRS; Rgs6; mouse.
DR PRO; PR:Q9Z2H2; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9Z2H2; protein.
DR Bgee; ENSMUSG00000021219; Expressed in cortical plate and 76 other tissues.
DR ExpressionAtlas; Q9Z2H2; baseline and differential.
DR Genevisible; Q9Z2H2; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR CDD; cd00068; GGL; 1.
DR CDD; cd08737; RGS_RGS6; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 4.10.260.10; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR036284; GGL_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR037956; RGS6_RGS.
DR InterPro; IPR040759; RGS_DHEX.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00631; G-gamma; 1.
DR Pfam; PF00615; RGS; 1.
DR Pfam; PF18148; RGS_DHEX; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00224; GGL; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF48670; SSF48670; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Nucleus; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..472
FT /note="Regulator of G-protein signaling 6"
FT /id="PRO_0000204193"
FT DOMAIN 40..115
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 261..330
FT /note="G protein gamma"
FT DOMAIN 336..451
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
SQ SEQUENCE 472 AA; 54531 MW; 94EB9AD49764196C CRC64;
MAQGSGDQRA VGIADPEESS PNMIVYCKIE DIITKMQDDK TGGVPIRTVK SFLSKIPSVV
TGTDIVQWLM KNLSIEDPVE AIHLGSLIAA QGYIFPISDH VLTMKDDGTF YRFQAPYFWP
SNCWEPENTD YAIYLCKRTM QNKARLELAD YEAENLARLQ RAFARKWEFI FMQAEAQVKI
DRKKDKTERK ILDSQERAFW DVHRPVPGCV NTTEMDIRKC RRLKNPQKVK KSVYGVTDET
QSQSPVHIPS QPIRKTTKDD IRKQITFLNA QIDRHCLKMS KVAESLIAYT EQYVEYDPFI
TPAEPSNPWI SDDITLWDIE MSKEPSQQRV KRWGFSFDEI LKDQVGRDQF LRFLESEFSS
ENLRFWLSVQ DLKKQPLQDV AKRVEEIWQE FLAPGAPSAI NLDSHSYEIT SQNVKDGGRY
TFEDAQEHIY KLMKSDSYAR FLRSNAYQDL LLAKKKGKSL AGKRLTGLMQ SS
